2no2: Difference between revisions
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[[Image:2no2.gif|left|200px]] | [[Image:2no2.gif|left|200px]] | ||
'''Crystal structure of the DLLRKN-containing coiled-coil domain of Huntingtin-interacting protein 1''' | {{Structure | ||
|PDB= 2no2 |SIZE=350|CAPTION= <scene name='initialview01'>2no2</scene>, resolution 2.800Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= HIP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Crystal structure of the DLLRKN-containing coiled-coil domain of Huntingtin-interacting protein 1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NO2 is a [ | 2NO2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NO2 OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding., Ybe JA, Mishra S, Helms S, Nix J, J Mol Biol. 2007 Mar 16;367(1):8-15. Epub 2006 Dec 23. PMID:[http:// | Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding., Ybe JA, Mishra S, Helms S, Nix J, J Mol Biol. 2007 Mar 16;367(1):8-15. Epub 2006 Dec 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17257618 17257618] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: clathrin light chain binding; hip1 coiled-coil domain; endocytosis; clathrin self-assembly]] | [[Category: clathrin light chain binding; hip1 coiled-coil domain; endocytosis; clathrin self-assembly]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:48:48 2008'' | ||
Revision as of 18:48, 20 March 2008
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| , resolution 2.800Å | |||||||
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| Gene: | HIP1 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the DLLRKN-containing coiled-coil domain of Huntingtin-interacting protein 1
OverviewOverview
Huntingtin interacting protein 1 (HIP1) is a member of a family of proteins whose interaction with Huntingtin is critical to prevent cells from initiating apoptosis. HIP1, and related protein HIP12/1R, can also bind to clathrin and membrane phospholipids, and HIP12/1R links the CCV to the actin cytoskeleton. HIP1 and HIP12/1R interact with the clathrin light chain EED regulatory site and stimulate clathrin lattice assembly. Here, we report the X-ray structure of the coiled-coil domain of HIP1 (residues 482-586) that includes residues crucial for binding clathrin light chain. The dimeric HIP1 crystal structure is partially splayed open. The comparison of the HIP1 model with coiled-coil predictions revealed the heptad repeat in the dimeric trunk (S2 path) is offset relative to the register of the heptad repeat from the N-terminal portion (S1 path) of the molecule. Furthermore, surface analysis showed there is a third hydrophobic path (S3) running parallel with S1 and S2. We present structural evidence supporting a role for the S3 path as an interaction surface for clathrin light chain. Finally, comparative analysis suggests the mode of binding between sla2p and clathrin light chain may be different in yeast.
DiseaseDisease
Known disease associated with this structure: Prostate cancer, progression of OMIM:[601767]
About this StructureAbout this Structure
2NO2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure at 2.8 A of the DLLRKN-containing coiled-coil domain of huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding., Ybe JA, Mishra S, Helms S, Nix J, J Mol Biol. 2007 Mar 16;367(1):8-15. Epub 2006 Dec 23. PMID:17257618
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